The human and mouse replication-dependent histone genes

Genomics

Volumn 80, Issue 5, 2002, Pages 487-498

  Marzluff, William F ^a,b   Gongidi, Preetam ^a   Woods, Keith R ^a   Jin, Jianping ^a   Maltais, Lois J ^c  

^a UNIVERSITY OF NORTH CAROLINA   (United States)

^b UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^c JACKSON LABORATORY   (United States)

Author keywords

Gene family; Histone; Histone mRNA; Human genome; Mouse genome

Indexed keywords

HISTONE; MESSENGER RNA; PROTEIN; PURINE; SMALL NUCLEAR RNA;

ALLELE; ARTICLE; CHROMOSOME 1; CHROMOSOME 11; CHROMOSOME 13; CHROMOSOME 3; CHROMOSOME 6; GENE CLUSTER; GENE LOCATION; GENE REPLICATION; GENE SEQUENCE; GENE STRUCTURE; GENETIC ANALYSIS; GENETIC CODE; MULTIGENE FAMILY; PRIORITY JOURNAL; PROTEIN ANALYSIS; STRUCTURE ANALYSIS; AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; CHROMOSOME MAP; GENETICS; HUMAN; MOLECULAR GENETICS; MOUSE; NOMENCLATURE; PHYLOGENY;

AMINO ACID SEQUENCE; ANIMALS; CHROMOSOME MAPPING; CHROMOSOMES, HUMAN, PAIR 6; HISTONES; HUMANS; MICE; MOLECULAR SEQUENCE DATA; MULTIGENE FAMILY; PHYLOGENY; RNA, MESSENGER; TERMINOLOGY;

EID: 0036429193     PISSN: 08887543     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0888-7543(02)96850-3     Document Type: Article

References (56)

1. Dominski, Z., and Marzluff, W. F. (1999). Formation of the 3′ end of histone mRNA. Gene 239: 1-14.
2. Pandey, N. B., Chodchoy, N., Liu, T.-J., and Marzluff, W. F. (1990). Introns in histone genes alter the distribution of 3′ ends. Nucleic Acids Res. 18: 3161-3170.
3. Mowry, K. L., and Steitz, J. A. (1987). Identification of the human U7 snRNP as one of several factors involved in the 3′ end maturation of histone premessenger RNA's. Science 238: 1682-1687.
4. Hancock, R. (1969). Conservation of histones in chromatin during growth and mitosis and in vitro. J. Mol. Biol. 40: 457-467.
5. Harris, M. E.,et al. (1991). Regulation of histone mRNA in the unperturbed cell cycle: Evidence suggesting control at two posttranscriptional steps. Mol. Cell. Biol. 11: 2416-2424.
6. Mannironi, C., Bonner, W. M., and Hatch, C. L. (1989). H2A.X. a histone isoprotein with a conserved C-terminal sequence, is encoded by a novel mRNA with both DNA replication type and polyA 3′ processing signals. Nucleic Acids Res. 17: 9113-9126.
7. Hatch, C. L., and Bonner, W. M. (1990). The human histone H2A.Z gene. Sequence and regulation. J. Biol. Chem. 265: 15211-15218.
8. Brush, D., Dodgson, J. B., Choi, O. R., Stevens, P. W., and Engel, J. D. (1985). Replacement variant histone genes contain intervening sequences. Mol. Cell. Biol. 5: 1307-1317.
9. Pehrson, J. R., and Cole, R. D. (1982). Histone H1 subfractions and H1° turnover at different rates in nondividing cells. Biochemistry 21: 456-460.
10. Tanaka, M., Hennebold, J. D., Macfarlane, J., and Adashi, E. Y. (2001). A mammalian oocyte-specific linker histone gene H1oo: Homology with the genes for the oocyte-specific cleavage stage histone (cs-H1) of sea urchin and the B4/H1M histone of the frog. Development 128: 655-664.
11. Albig, W., and Doenecke, D. (1997). The human histone gene cluster at the D6S105 locus. Hum. Genet. 101: 284-294.
12. Albig, W., Kioschis, P., Poustka, A., Meergans, K., and Doenecke, D. (1997). Human histone gene organization: Nonregular arrangement within a large cluster. Genomics 40: 314-322.
13. Wang, Z.-F.,et al. (1996). Characterization of the mouse histone gene cluster on chromosome 13: 45 Histone genes in three patches spread over one megabase. Genome Res. 6: 688-701.
14. Wang, Z.-F.,et al. (1996). Characterization of the 55 kilobase mouse histone gene cluster on chromosome 3. Genome Res. 6: 702-714.
15. Zweidler, A. (1984). Core histone variants of the mouse: Primary structure and expression. InHistone Genes: Structure, Organization and Regulation (G. Stein, W. Stein, and W. F. Marzluff, Eds.), pp. 373-395. John Wiley and Sons, New York.
16. Lennox, R. W., and Cohen, L. H. (1983). The histone H1 complements of dividing and nondividing cells of the mouse. J. Biol. Chem. 258: 262-268.
17. Wang, Z.-F., Sirotkin, A. M., Buchold, G. M., Skoultchi, A. I., and Marzluff, W. F. (1997). The mouse histone H1 genes: gene organization and differential regulation. J. Mol. Biol. 271: 124-138.
18. Feder, J. N.,et al. (1996). A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis. Nat. Genet. 13: 399-408.
19. Albig, W., Ebentheuer, J., Klobeck, G., Kunz, J., and Doenecke, D. (1996). A solitary human H3 histone gene on chromosome 1. Hum. Genet. 97: 486-491.
20. Witt, O., Albig, W., and Doenecke, D. (1996). Testis-specific expression of a novel human H3 histone gene. Exp. Cell Res. 229: 301-306.
21. Smith, M. M., and Murray, K. (1983). Yeast H3 and H4 histone messenger RNAs are transcribed from two non-allelic gene sets. J. Mol. Biol. 169: 641-661.
22. Lifton, R. P., Goldberg, M. L., Karp, R. W., and Hogness, D. S. (1978). The organization of the histone genes in Drosophila melanogaster: Functional and evolutionary implications. Cold Spring Harb. Symp. Quant. Biol. 42: 1047-1051.
23. Pettitt, J., Crombie, C., Schümperli, D., and Müller, B. (2002). The Caenorhabditis elegans histone hairpin-binding protein is required for core histone expression and is essential for embryonic and postembryonic cell division. J. Cell Sci. 115: 857-866.
24. Cohn, R. H., Lowry, J. C., and Kedes, L. H. (1976). Histone genes of the sea urchin (S. purpuratus) cloned in E. coli; order, polarity and strandedness of the five histone coding and spacer regions. Cell 9: 147-161.
25. Nakayama, T., Takechi, S., and Takami, Y. (1993). The chicken histone gene family. Comp. Biochem. Physiol. 104B: 635-639.
26. Stephenson, E. C., Erba, H. P., and Gall, J. G. (1981). Characterization of a cloned histone gene cluster of the newtNotophthalamus viridescens. Nucleic Acids Res. 9: 2281-2295.
27. Perry, M., Thomsen, G. H., and Roeder, R. G. (1985). Genomic organization and nucleotide sequence of two distinct histone clusters fromXenopus laevis. J. Mol. Biol. 185: 479-499.
28. Cheng, G., Nandi, A., Clerk, S., and Skoultchi, A. I. (1989). Different 3′-end processing produces two independently regulated mRNAs from a single H1 histone gene. Proc. Natl. Acad. Sci. USA 86: 7002-7006.
29. Collart, D.,et al. (1992). A human histone H2B.1 variant gene, located on chromosome 1, utilizes alternative 3′ end processing. J. Cell. Biochem. 50: 374-385.
30. Lennox, R. W., and Cohen, L. H. (1984). The alterations in H1 histone complement during mouse spermatogenesis and their significance for H1 subtype function. Dev. Biol. 103: 80-84.
31. Choi, Y. C., Gu, W., Hecht, N. B., Feinberg, A. P., and Chae, C. B. (1996). Molecular cloning of mouse somatic and testis-specific H2B histone genes containing a methylated CpG island. DNA Cell Biol. 15: 495-504.
32. Ivanova, V. S., Zimonjic, D., Popescu, N., and Bonner, W. M. (1994). Chromosomal localization of the human histone H2A.X gene to 11q23.2-q23.3 by fluorescence in situ hybridization. Hum. Genet. 94: 303-306.
33. Whitfield, M. L.,et al. (2000). Stem-loop binding protein, the protein that binds the 3′ end of histone mRNA, is cell cycle regulated by both translational and posttranslational mechanisms. Mol. Cell. Biol. 20: 4188-4198.
34. Albig, W.,et al. (1995). The human replacement histone H3.3B gene (H3F3B). Genomics 30: 264-272.
35. Akhmanova, A., Miedema, K., and Hennig, W. (1996). Identification and characterization of the Drosophila histone H4 replacement gene. FEBS Lett. 388: 219-222.
36. Fretzin, S., Allan, B. D., Van Daal, A., and Elgin, S. C. R. (1991). ADrosophila melanogaster H3.3 cDNA encodes a histone variant identical with the vertebrate H3.3. Gene 107: 341-342.
37. Ahmad, K., and Henikoff, S. (2002). The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly. Mol. Cell 9: 1191-1200.
38. Debry, R. W., and Marzluff, W. F. (1994). Selection on silent sites in the rodent H3 his-tone gene family. Genetics 138: 191-202.
39. Graves, R. A., Pandey, N. B., Chodchoy, N., and Marzluff, W. F. (1987). Translation is required for regulation of histone mRNA degradation. Cell 48: 615-626.
40. Lanzotti, D. J., Kaygun, H., Yang, X., Duronio, R. J., and Marzluff, W. F. (2002). Developmental control of histone mRNA and dSLBP synthesis during Drosophila embryogenesis and the role of dSLBP in histone mRNA 3′ processing in vivo. Mol. Cell. Biol. 22: 2267-2282.
41. Matera, A. G. (1998). Of coiled bodies, gems, and salmon. J. Cell. Biochem. 70: 181-192.
42. Fletcher, C., Heintz, N., and Roeder, R. G. (1987). Purification and characterization of OTF-1, a transcription factor regulating cell cycle expression of a human histone H2b gene. Cell 51: 773-781.
43. Eliassen, K. A., Baldwin, A., Sikorski, E. M., and Hurt, M. M. (1998). Role for a YY1 binding site in replication-dependent mouse histone gene expression. Mol. Cell. Biol. 18: 7106-7118.
44. NPAT by cyclin E/Cdk2 in Cajal bodies promotes histone gene transcription. Genes Dev. 14: 2298-2313.
45. Zhao, J. Y.,et al. (2000). NPAT links cyclin E-Cdk2 to the regulation of replication-dependent histone gene transcription. Genes Dev. 14: 2283-2297.
46. El-Hodiri, H. M., and Perry, M. (1995). Interaction of the CCAAT displacement protein with shared regulatory elements required for transcription of paired histone genes. Mol. Cell. Biol. 15: 3587-3596.
47. 1/S phase cell cycle transition point independent of transcription factor E2F. Proc. Natl. Acad. Sci. USA 93: 11516-11521.
48. Brown, D. T., Yang, Y.-S., and Sittman, D. B. (1988). Histone gene switching in murine erythroleukemia cells is differentiation specific and occurs without loss of cell cycle regulation. Mol. Cell. Biol. 8: 4406-4415.
49. Engel, J. D., and Tanimoto, K. (2000). Looping, linking, and chromatin activity: New insights into α-globin locus regulation. Cell 100: 499-502.
50. Liu, T.-J., Liu, L., and Marzluff, W. F. (1987). Mouse histone H2a and H2b genes; four functional genes and a pseudogene undergoing gene conversion with a closely linked functional gene. Nucleic Acids Res. 15: 3023-3039.
51. Sittman, D. B., Graves, R. A., and Marzluff, W. F. (1983). Structure of a cluster of mouse histone genes. Nucleic Acids Res. 11: 6679-6697.
52. Brown, V. D., Wang, Z.-F., Williams, A. S., and Marzluff, W. F. (1996). Structure of a cluster of mouse histone genes.Biochim. Biophys. Acta Gene Struct. Expr. 1306: 17-22.
53. Gruber, A.,et al. (1990). Structure of a mouse histone-encoding gene cluster. Gene 95: 303-304.
54. Seiler-Tuyns, A., and Birnstiel, M. L. (1981). Structure and expression in L-cells of a cloned H4 histone gene of the mouse. J. Mol. Biol. 157: 607-625.
55. Meier, V. S., Böhni, R., and Schümperli, D. (1989). Nucleotide sequence of two mouse histone H4 genes. Nucleic Acids Res. 17: 795.
56. Akasaka, T.,et al. (1997). A recurring translocation, t(3;6)(q27;p21), in non-Hodgkin's lymphoma results in replacement of the 5′ regulatory region of BCL6 with a novel H4 histone gene. Cancer Res. 57: 7-12.